Despite having an optimal sample for crystallization, obtaining crystals can be an arduous and unpredictable goal. The most important approaches to overcome this bottleneck were the discovery of appropriate precipitants, new methods of preparation of macromolecule samples, new methods of carrying out crystallization experiments but above all the increase of crystallization efficiency through automation.
In the developing brain, cell-surface proteins play crucial roles, but their protein-protein interaction network remains largely unknown. A proteomic screen identified 200 interactions, 89 of which were not previously published. Among these interactions, we find that the IgLONs, a family of five cell-surface neuronal proteins implicated in various human disorders, interact as homo- and heterodimers. We reveal their interaction patterns and report the dimeric crystal structures of Neurotrimin (NTRI), IgLON5, and the neuronal growth regulator 1 (NEGR1)/IgLON5 complex.
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